IR@PKUHSC  > 北京大学基础医学院  > 生物物理学系
学科主题基础医学
PrP106-126 peptide disrupts lipid membranes: Influence of C-terminal amidation
Zheng, Wenfu; Wang, Lijun; Hong, Yuankai; Sha, Yinlin1
关键词PrP106-126 C-terminal amidation Supported lipid bilayers Large unilamellar vesicles Flat high-rise domains Atomic force microscopy Surface plasmon resonance
刊名BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
2009-02-06
DOI10.1016/j.bbrc.2008.12.049
379期:2页:298-303
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology ; Biophysics
资助者NSFC ; NSFC
研究领域[WOS]Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]PRION PROTEIN-FRAGMENT ; SURFACE-PLASMON RESONANCE ; ATOMIC-FORCE MICROSCOPY ; NEUROTOXICITY ; RESIDUES-106-126 ; CONVERSION ; LIPOSOMES ; OXIDATION ; BILAYERS ; BINDING
英文摘要

PrP106-126 is located within the important domain concerning membrane related conformational conversion of human Prion protein (from cellular isoform PrPC to scrapie isoform PrPSc). Recent advances reveal that the pathological and physicochemical properties of PrP106-126 peptide are very sensitive to its N-terminal amidation, however, the detailed mechanism remains unclear. In this work, we studied the interactions of the PrP106-126 isoforms (PrP106-126(CONH2) and PrP106-426(COOH)) with the neutral lipid bilayers by atomic force microscopy, surface plasmon resonance and fluorescence spectroscopy. The membrane structures were disturbed by the two isoforms in a similarly stepwise process. The distinct morphological changes of the membrane were characterized by formation of semi-penetrated defects and sigmoidal growth of flat high-rise domains on the supported lipid bilayers. However, PrP106-126(COOH) displayed a higher peptide-lipid binding affinity than PrP106-126(CONH2) (similar to 2.9 times) and facilitated the peptide-lipid interactions by shortening the lag time. These results indicate that the C-terminal amidation may influence the pathological actions of PrP106-126 by lowering the interaction potentials with lipid membranes. (c) 2008 Elsevier Inc. All rights reserved.

语种英语
所属项目编号20273002 ; 20673001
资助者NSFC ; NSFC
WOS记录号WOS:000262924300026
Citation statistics
Cited Times:9[WOS]   [WOS Record]     [Related Records in WOS]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/59382
Collection北京大学基础医学院_生物物理学系
作者单位1.Peking Univ, Single Mol & Nanobiol Lab, Dept Biophys, Sch Basic Med Sci, Beijing 100191, Peoples R China
2.Peking Univ, Ctr Prot Sci, Beijing 100191, Peoples R China
3.Peking Univ, Biomed X Ctr, Beijing 100191, Peoples R China
Recommended Citation
GB/T 7714
Zheng, Wenfu,Wang, Lijun,Hong, Yuankai,et al. PrP106-126 peptide disrupts lipid membranes: Influence of C-terminal amidation[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2009,379(2):298-303.
APA Zheng, Wenfu,Wang, Lijun,Hong, Yuankai,&Sha, Yinlin.(2009).PrP106-126 peptide disrupts lipid membranes: Influence of C-terminal amidation.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,379(2),298-303.
MLA Zheng, Wenfu,et al."PrP106-126 peptide disrupts lipid membranes: Influence of C-terminal amidation".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 379.2(2009):298-303.
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